2.02012-05-31 10:22:12 -06002015-09-13 12:56:06 -0600ECMDB00158M2MDB000060L-TyrosineTyrosine (Tyr, Y) or 4-hydroxyphenylalanine is a non-essential amino acid with a polar side group. Its codons are UAC and UAU. Aside from being a proteogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinases (so-called receptor tyrosine kinases). Phosphorylation of the hydroxyl group changes the activity of the target protein. (Wikipedia) L-Tyrosine is the enantiomer of tyrosine (the other being D-tyrosine) that is used in building proteins.(-)-a-Amino-p-hydroxyhydrocinnamate(-)-a-Amino-p-hydroxyhydrocinnamic acid(-)-alpha-Amino-p-hydroxyhydrocinnamate(-)-alpha-Amino-p-hydroxyhydrocinnamic acid(-)-α-amino-P-Hydroxyhydrocinnamate(-)-α-amino-P-Hydroxyhydrocinnamic acid(S)-(-)-Tyrosine(S)-2-Amino-3-(p-hydroxyphenyl)propionate(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid(S)-3-(p-Hydroxyphenyl)alanine(S)-a-amino-4-hydroxy-Benzenepropanoate(S)-a-amino-4-hydroxy-Benzenepropanoic acid(S)-a-Amino-4-hydroxybenzenepropanoate(S)-a-Amino-4-hydroxybenzenepropanoic acid(S)-alpha-amino-4-hydroxy-Benzenepropanoate(S)-alpha-amino-4-hydroxy-Benzenepropanoic acid(S)-alpha-Amino-4-hydroxybenzenepropanoate(S)-alpha-Amino-4-hydroxybenzenepropanoic acid(S)-Tyrosine(S)-α-amino-4-Hydroxy-benzenepropanoate(S)-α-amino-4-Hydroxy-benzenepropanoic acid(S)-α-amino-4-Hydroxybenzenepropanoate(S)-α-amino-4-Hydroxybenzenepropanoic acid2-Amino-3-(4-hydroxyphen yl)-2-amino-3-(4-hydroxyphenyl)-Propanoate2-Amino-3-(4-hydroxyphen yl)-2-amino-3-(4-hydroxyphenyl)-Propanoic acid3-(4-Hydroxyphenyl)-L-alanine4-Hydroxy-L-PhenylalanineBenzenepropanoateBenzenepropanoic acidL-p-TyrosineL-TyrosineP-TyrosineTyrTyrosineYC9H11NO3181.1885181.073893223(2S)-2-amino-3-(4-hydroxyphenyl)propanoic acidL-tyrosine60-18-4N[C@@H](CC1=CC=C(O)C=C1)C(O)=OInChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1OUYCCCASQSFEME-QMMMGPOBSA-NSolidCytosolExtra-organismPeriplasmlogp-2.39logs-1.37solubility7.67e+00 g/lmelting_point343 oClogp-1.5pka_strongest_acidic2pka_strongest_basic9.19iupac(2S)-2-amino-3-(4-hydroxyphenyl)propanoic acidaverage_mass181.1885mono_mass181.073893223smilesN[C@@H](CC1=CC=C(O)C=C1)C(O)=OformulaC9H11NO3inchiInChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1inchikeyOUYCCCASQSFEME-QMMMGPOBSA-Npolar_surface_area83.55refractivity47.1polarizability18.01rotatable_bond_count3acceptor_count4donor_count3physiological_charge0formal_charge0Tyrosine metabolismec00350Phenylalanine metabolismThe pathways of the metabolism of phenylalaline begins with the conversion of chorismate to prephenate through a P-protein (chorismate mutase:pheA). Prephenate then interacts with a hydrogen ion through the same previous enzyme resulting in a release of carbon dioxide, water and a phenolpyruvic acid. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosine.
Phenolpyruvic acid can also be obtained from a reversivle reaction with ammonia, a reduced acceptor and a D-amino acid dehydrogenase, resulting in a water, an acceptor and a D-phenylalanine, which can be then transported into the periplasmic space by aromatic amino acid exporter.
L-phenylalanine also interacts in two reversible reactions, one involved with oxygen through a catalase peroxidase resulting in a carbon dioxide and 2-phenylacetamide. The other reaction involved an interaction with oxygen through a phenylalanine aminotransferase resulting in a oxoglutaric acid and phenylpyruvic acid.
L-phenylalanine can be imported into the cytoplasm through an aromatic amino acid:H+ symporter AroP.
The compound can also be imported into the periplasmic space through a transporter: L-amino acid efflux transporter.PW000921ec00360MetabolicPhenylalanine, tyrosine and tryptophan biosynthesisec00400Novobiocin biosynthesisec00401Cyanoamino acid metabolismec00460Aminoacyl-tRNA biosynthesisec00970Thiamine metabolismec00730Ubiquinone and other terpenoid-quinone biosynthesisec00130Metabolic pathwayseco01100inner membrane transportlist of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports addedPW000786MetabolictRNA Charging 2This pathway groups together all E. coli tRNA charging reactions.PW000803MetabolictRNA chargingThis pathway groups together all E. coli tRNA charging reactions.PW000799Metabolictyrosine biosynthesisThe pathways of biosynthesis of phenylalaline and tyrosine are intimately connected. First step of both pathways is the conversion of chorismate to prephenate, the third step of both is the conversion of a ketoacid to the aminoacid through transamination. The two pathways differ only in the second step of their three-step reaction sequences: In the case of phenylalanine biosynthesi a dehydratase converts prephenate to phenylpyruvate(reaction occurs slowly in the absence of enzymic activity); in the case of tyrosine biosynthesis, a dehydrogenase converts prephenate to p-hydroxyphenylpyruvate. Also in both pathways the first two steps are catalyzed by two distinc active sites on a single protein. Thus the first step of each pathway can be catalyzed by two enzyme: those associated with both the phenylalanine specific dehydratase and the tyrosine specific dehydrogenase. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosinePW000806MetabolicThiazole Biosynthesis IThis pathway describes only the synthesis of the thiazole moiety of thiamin. Different variations of this pathway exist, this particular pathway describes the pathway that occurs in Escherichia coli K-12 and Salmonella enterica enterica serovar Typhimurium.
The biosynthesis of the thiazole moiety is complex. In Escherichia coli it involves six proteins, the products of the thiS, thiF, thiG, thiH, thiI, and iscS genes.
The process begins when IscS, a protein that is also involved in the biosynthesis of iron-sulfur clusters, catalyzes the transfer of a sulfur atom from cysteine to a ThiI sulfur-carrier protein, generating a an S-sulfanyl-[ThiI sulfur-carrier protein].
In a parallel route, the ThiF protein activates a ThiS sulfur-carrier protein by adenylation of its carboxy terminus, generating a carboxy-adenylated-[ThiS sulfur-carrier protein]. In a second reaction, which may also be catalyzed by ThiF, the sulfur from an S-sulfanyl-[ThiI sulfur-carrier protein] is transferred to ThiS, generating a thiocarboxy-[ThiS-Protein].
The final reaction of this pathway, which is catalyzed by the ThiG protein, requires three inputs: a thiocarboxy-[ThiS-Protein], 1-deoxy-D-xylulose 5-phosphate and 2-iminoacetate.
2-iminoacetate is formed in Escherichia coli from L-tyrosine by tyrosine lyase (ThiH), which forms a complex with ThiG.
For many years the products of this reaction was assumed to be 4-methyl-5-(β-hydroxyethyl)thiazole (thiazole). However, recent work performed with the thiazole synthase from Bacillus subtilis has shown that the actual product is the thiazole tautomer 2-[(2R,5Z)-(2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate. While in Bacillus a dedicated thiazole tautomerase converts this product into a different tautomer (2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate), most of the proteobacteria lack the tautomerase. (EcoCyc)PW002041Metabolicthiazole biosynthesis I (E. coli)PWY-6892tRNA chargingTRNA-CHARGING-PWYtyrosine biosynthesis ITYRSYNSpecdb::CMs383Specdb::CMs384Specdb::CMs385Specdb::CMs386Specdb::CMs387Specdb::CMs388Specdb::CMs1602Specdb::CMs1669Specdb::CMs2619Specdb::CMs30212Specdb::CMs30317Specdb::CMs30318Specdb::CMs30319Specdb::CMs30614Specdb::CMs30740Specdb::CMs30773Specdb::CMs31030Specdb::CMs31031Specdb::CMs37328Specdb::CMs173009Specdb::CMs1051730Specdb::CMs1051732Specdb::CMs1051734Specdb::CMs1051736Specdb::CMs1051738Specdb::EiMs1974Specdb::NmrOneD1117Specdb::NmrOneD1175Specdb::NmrOneD4862Specdb::NmrOneD4863Specdb::NmrOneD4864Specdb::NmrOneD4865Specdb::NmrOneD5912Specdb::NmrOneD5913Specdb::NmrOneD5914Specdb::NmrOneD5915Specdb::NmrOneD5916Specdb::NmrOneD5917Specdb::NmrOneD5918Specdb::NmrOneD5919Specdb::NmrOneD5920Specdb::NmrOneD5921Specdb::NmrOneD5922Specdb::NmrOneD5923Specdb::NmrOneD5924Specdb::NmrOneD5925Specdb::NmrOneD5926Specdb::NmrOneD5927Specdb::NmrOneD5928Specdb::NmrOneD5929Specdb::NmrOneD5930Specdb::MsMs245Specdb::MsMs246Specdb::MsMs247Specdb::MsMs3155Specdb::MsMs3156Specdb::MsMs3157Specdb::MsMs3158Specdb::MsMs3159Specdb::MsMs3160Specdb::MsMs3161Specdb::MsMs3162Specdb::MsMs3163Specdb::MsMs3164Specdb::MsMs3165Specdb::MsMs3166Specdb::MsMs3167Specdb::MsMs3168Specdb::MsMs3169Specdb::MsMs3170Specdb::MsMs3171Specdb::MsMs3172Specdb::MsMs3173Specdb::MsMs3174Specdb::MsMs3175Specdb::MsMs3176Specdb::NmrTwoD974Specdb::NmrTwoD1176HMDB0015860575833C0008217895TYRTYR_LFZW_DHHTyrosineKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72.18402659van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). 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"Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597.17379776Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4.19212411Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7.12097436Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. 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Microbiological synthesis of L-tyrosine and 3,4-dihydroxyphenyl-L-alanine. I. Distribution of tyrosine phenol lyase in microorganisms. Agricultural and Biological Chemisthttp://hmdb.ca/system/metabolites/msds/000/000/109/original/HMDB00158.pdf?1358894696Aspartate aminotransferaseP00509AAT_ECOLIaspChttp://ecmdb.ca/proteins/P00509.xmlAromatic-amino-acid aminotransferaseP04693TYRB_ECOLItyrBhttp://ecmdb.ca/proteins/P04693.xmlHistidinol-phosphate aminotransferaseP06986HIS8_ECOLIhisChttp://ecmdb.ca/proteins/P06986.xmlPeriplasmic AppA proteinP07102PPA_ECOLIappAhttp://ecmdb.ca/proteins/P07102.xmlClass B acid phosphataseP0AE22APHA_ECOLIaphAhttp://ecmdb.ca/proteins/P0AE22.xmlTyrosyl-tRNA synthetaseP0AGJ9SYY_ECOLItyrShttp://ecmdb.ca/proteins/P0AGJ9.xmlThiazole synthaseP30139THIG_ECOLIthiGhttp://ecmdb.ca/proteins/P30139.xmlDehydroglycine synthaseP30140THIH_ECOLIthiHhttp://ecmdb.ca/proteins/P30140.xmlUncharacterized amino-acid ABC transporter ATP-binding protein yecCP37774YECC_ECOLIyecChttp://ecmdb.ca/proteins/P37774.xmlInner membrane amino-acid ABC transporter permease protein yecSP0AFT2YECS_ECOLIyecShttp://ecmdb.ca/proteins/P0AFT2.xmlTyrosine-specific transport proteinP0AAD4TYRP_ECOLItyrPhttp://ecmdb.ca/proteins/P0AAD4.xmlAromatic amino acid transport protein AroPP15993AROP_ECOLIaroPhttp://ecmdb.ca/proteins/P15993.xmlPhenylalanine-specific permeaseP24207PHEP_ECOLIphePhttp://ecmdb.ca/proteins/P24207.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlInner membrane protein yddGP46136YDDG_ECOLIyddGhttp://ecmdb.ca/proteins/P46136.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlalpha-Ketoglutarate + L-Tyrosine <> 4-Hydroxyphenylpyruvic acid + L-GlutamateR00734Adenosine triphosphate + tRNA(Tyr) + L-Tyrosine + tRNA(Tyr) <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr) + L-Tyrosyl-tRNA(Tyr)R02918S-Adenosylmethionine + NADPH + L-Tyrosine > p-Cresol + 5'-Deoxyadenosine + Dehydroglycine + Hydrogen ion + L-Methionine + NADPWater + Phosphotyrosine > Phosphate + L-TyrosineAdenosine triphosphate + L-Tyrosine + tRNA(Tyr) <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr)R02918C15815 + L-Tyrosine + Iminoglycine <> 4-Methyl-5-(2-phosphoethyl)-thiazoleR07465L-Tyrosine + S-Adenosylmethionine + a reduced electron acceptor > Dehydroglycine + p-Cresol + 5'-Deoxyadenosine + L-Methionine + an oxidized electron acceptor + Hydrogen ionRXN-11319L-Tyrosine + Oxoglutaric acid <> 4-Hydroxyphenylpyruvic acid + L-GlutamateTYRAMINOTRANS-RXNAdenosine triphosphate + L-Tyrosine + tRNA(Tyr) > Adenosine monophosphate + Pyrophosphate + L-tyrosyl-tRNA(Tyr)L-Tyrosine + S-adenosyl-L-methionine + reduced acceptor > 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + acceptor +2 Hydrogen ionL-Tyrosine + S-Adenosylmethionine + NADPH <> 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ionR10246 L-Tyrosine + Adenosine triphosphate + Hydrogen ion + tRNA(Tyr) + L-Tyrosine > Adenosine monophosphate + Pyrophosphate + L-tyrosyl-tRNA(Tyr)PW_R0028354-hydroxyphenylpyruvate + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Tyrosine + L-TyrosinePW_R002858L-Tyrosine + NADPH + S-adenosyl-L-methionine + L-Tyrosine + NADPH > Hydrogen ion + NADP + L-Methionine + 5'-Deoxyadenosine + p-Cresol + 2-iminoacetatePW_R005174L-Tyrosine + S-adenosyl-L-methionine + NADPH > Dehydroglycine + 4-Methylcatechol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ionPW_R005962C15815 + L-Tyrosine + 2-iminoacetate <>4 4-Methyl-5-(2-phosphoethyl)-thiazoleAdenosine triphosphate + tRNA(Tyr) + L-Tyrosine <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr)C15815 + L-Tyrosine + 2-iminoacetate <>4 4-Methyl-5-(2-phosphoethyl)-thiazoleAdenosine triphosphate + tRNA(Tyr) + L-Tyrosine <> Adenosine monophosphate + Pyrophosphate + L-Tyrosyl-tRNA(Tyr)Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseShake flask and filter culture28.9uM0.037 oCK12 NCM3722Mid-Log Phase1156000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolShake flask and filter culture87.4uM0.037 oCK12 NCM3722Mid-Log Phase3496000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateShake flask and filter culture52.2uM0.037 oCK12 NCM3722Mid-Log Phase2088000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.1956162148 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37.8uM0.037 oCBW25113Stationary Phase, glucose limited1512000Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597.17379776Luria-Bertani (LB) mediaShake flask76.8uMtrue6.2437 oCBL21 DE3Stationary phase cultures (overnight culture)30720024954Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911